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The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR
Open accessAbstract
The serine/threonine kinase ULK1 is a mammalian homolog of Atg1, part of the Atg1 kinase complex, which is the most upstream component of the core autophagy machinery conserved from yeast to mammals. In budding yeast, activity of the Atg1 kinase complex is inhibited by TORC1 (target of rapamycin complex 1), but how the counterpart ULK1 complex in mammalian cells is regulated has been unknown. Our laboratories recently discovered that AMPK associates with, and directly phosphorylates, ULK1 on several sites and this modification is required for ULK1 activation after glucose deprivation. In contrast, when nutrients are plentiful, the mTORC1 complex phosphorylates ULK1, preventing its association and activation by AMPK. These studies have revealed a molecular mechanism of ULK1 regulation by nutrient signals via the actions of AMPK and mTORC1.
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“Under glucose starvation, AMPK apparently promotes autophagy by directly activating ULK1 through phosphorylation, although the exact AMPK-mediated ULK1 phosphorylation site(s) remains controversial (Table 2) [665, 669-671].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [671]
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“Endurance training has been shown to inhibit mTOR/p70 S6K signaling and reduce IRS1 serine phosphorylation in rat skeletal muscle [157], and recent studies have demonstrated that AMPK is involved in the suppression of mTOR signaling [39].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [39]
In the citing paper
“Presumably, AMPK antagonizes the autophagy-inhibitory effect of amino acids (at the level of phagophore assembly) by phosphorylating proteins involved in MTORC1 signaling, such as TSC2 [668] and RPTOR/raptor [668] as well as the MTORC1 target ULK1 (see below) [669-671].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [671]
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AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
Self-citationPhosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600
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Zhang, J., Andersen, J.-P., Sun, H., Liu, X., Sonenberg, N., Nie, J., & Shi, Y. (2020) · EMBO Reports · doi:10.15252/embr.201949898 · Cited by 28
Mokhtari, B., & Badalzadeh, R. (2022) · Molecular Biology Reports · doi:10.1007/s11033-022-07837-9 · Cited by 28
Lu, Y., Xu, J., Li, Y., Wang, R., Dai, C., Zhang, B., Zhang, X., Xu, L., Tao, Y., Han, M., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.ade8647 · Cited by 29
de Theije, C. C., Schols, A. M. W. J., Lamers, W. H., Neumann, D., Köhler, E., & LANGEN, R. C. J. (2018) · PLoS ONE · doi:10.1371/journal.pone.0203630 · Cited by 30
Zhang, M., Fang, L., Zhou, L., Molino, A., Valentino, M. R., Yang, S., Zhang, J., Li, Y., & Roth, M. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.004 · Cited by 28
Beauchamp, E. M., Kościuczuk, E. M., Serrano, R. M. T., Nanavati, D. M., Swindell, E. P., Viollet, B., O’Halloran, T. V., Altman, J. K., & Platanias, L. C. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0665-t · Cited by 28
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Chen, G., Gong, R., Yang, D., Zhang, G., Lü, A., Yan, S., Lin, S., & Bian, Z. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.203 · Cited by 28
Bi, S., Wang, H., & Kuang, W. (2018) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2018.07.005 · Cited by 27
Ost, M., Werner, F., Dokas, J., Klaus, S., & Voigt, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094689 · Cited by 27
Xiao, Q., Yang, Y., Qin, Y. H., He, Y., Chen, K., Zhu, J., Zhang, G., & Luo, J. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.006 · Cited by 27
Wei, Z., Yuan, Y., Jaouen, F., Ma, M., Hao, C., Zhang, Z., Chen, Q., Yuan, Z., Yu, L., Beurrier, C., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1179402 · Cited by 28
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Cho, S. W., Na, W., Choi, M., Kang, S. J., Lee, S., & Choi, C. Y. (2017) · PubMed · Cited by 27
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Melick, C. H., Meng, D., & Jewell, J. L. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ac120.012595 · Cited by 27
Sun, P., Zhong, Z., Lu, Q., Li, M., Chao, X., Chen, D., Hu, W., Luo, R., & He, J. (2020) · Modern Pathology · doi:10.1038/s41379-020-0554-8 · Cited by 30
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Barnaba, C., Broadbent, D. G., Kaminsky, E. G., Perez, G. I., & Schmidt, J. C. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202309145 · Cited by 28
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Khodakarami, A., Sáez, I., Mels, J., & Vı́lchez, D. (2015) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2015.00003 · Cited by 27
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Gordon, B. S., Liu, C., Steiner, J. L., Nader, G. A., Jefferson, L. S., & Kimball, S. R. (2016) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00159.2016 · Cited by 28
Mani, K. M., Javaheri, A., & Diwan, A. (2018) · Comprehensive physiology · doi:10.1002/cphy.c180005 · Cited by 29
Zhang, Z., Tan, R., Xiong, Z., Feng, Y., & Chen, L. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1562845 · Cited by 31
Mu, P., & Ramanathan, K. (2019) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2019.1638401 · Cited by 26
Roberson, P. A., Shimkus, K. L., Welles, J. E., Xu, D., Whitsell, A. L., Kimball, E. M., Jefferson, L. S., & Kimball, S. R. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00155.2020 · Cited by 29
Torres-Esquivel, C., Montiel, T., Flores‐Méndez, M., & Massieu, L. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.547215 · Cited by 26
Wang, X.-Y., Zhu, B.-R., Jia, Q., Li, Y., Wang, T., & Wang, H. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c04898 · Cited by 28
Bao, Y., Qian, C., Liu, M.-Y., Jiang, F., Jiang, X., Liu, H., Zhang, Z., Sun, F., Fu, N., Hou, Z., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1886767 · Cited by 25
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Janda, E., Martino, C., Riillo, C., Parafati, M., Lascala, A., Mollace, V., & Boutin, J. A. (2021) · Antioxidants · doi:10.3390/antiox10050776 · Cited by 26
Zhang, Z., Chen, L., Chen, X., Qin, Y., Tian, C., Dai, X., Meng, R., Zhong, Y., Liang, W., Shen, C., et al. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.10.001 · Cited by 26
Chen, W., Lv, L., Nong, Z., Chen, X., Pan, X., & Chen, C. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11497 · Cited by 27
Joshi, J. N., Lerner, A. D., Scallo, F., Grumet, A. N., Matteson, P. G., Millonig, J. H., & Valvezan, A. J. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114543 · Cited by 25
Steiner, J. L., Crowell, K. T., Kimball, S. R., & Lang, C. H. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00264.2015 · Cited by 26
Park, S.-W., Park, M. Y., Park, H. G., Lee, K. J., Kook, M.-S., Kim, W. J., & Jung, J. (2016) · International Endodontic Journal · doi:10.1111/iej.12616 · Cited by 26
Zhao, H., Chen, D., Cao, R., Wang, S., Yu, D., Liu, Y., Jiang, Y., Xu, M., Luo, J., & Wang, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-26856-w · Cited by 26
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Lu, Y., Wang, S., Cai, S., Gu, X., Wang, J., Yang, Y., Hu, Z., Zhang, X.-H., Ye, Y., Shen, S., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02828-9 · Cited by 25
Zhuang, A., Chai, P., Wang, S., Zuo, S., Yu, J., Jia, S., Ge, S., Jia, R., Zhou, Y., Shi, W., et al. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.660 · Cited by 24
Jiang, S., Zou, Z., Nie, P., Wen, R., Yingying, X., & Tang, J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0132880 · Cited by 24
Weber, J. J., Sena, P. P., Singer, E., & Nguyen, H. P. (2019) · BioMed Research International · doi:10.1155/2019/4741252 · Cited by 27
Kim, H.-J., Jeon, B. T., Kim, I. M., Bennett, S. J., Lorch, C. M., Viana, M. P., Myers, J. F., Trupp, C. J., Whipps, Z. T., Kundu, M., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176130 · Cited by 24
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Liang, S., Li, X., Gao, C., & Zhang, L. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110799 · Cited by 25
Tsai, C.-H., Lii, C., Wang, T., Liu, K., Chen, H., Huang, C., & Li, C. (2021) · Food and Chemical Toxicology · doi:10.1016/j.fct.2021.112318 · Cited by 28
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Engin, A. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-63657-8_7 · Cited by 25
Park, S. M., Jung, E. H., Kim, J. K., Jegal, K. H., Park, C. A., Cho, I. J., & Kim, S. C. (2017) · Journal of Ginseng Research · doi:10.1016/j.jgr.2017.01.012 · Cited by 23
Self-citationMiao, X., Gu, Z., Liu, Y., Jin, M., Lu, Y., Gong, Y., Li, L., & Li, C. (2017) · Peptides · doi:10.1016/j.peptides.2017.07.006 · Cited by 24
Chen, Y., Chen, H.-J., Huang, B.-M., Chen, Y.-C., & Chang, C.-F. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8101664 · Cited by 23
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Khayati, K., Bhatt, V. D., Hu, Z. S., Fahumy, S., Luo, X., & Guo, J. Y. (2020) · eLife · doi:10.7554/elife.62377 · Cited by 21
Electroconvulsive seizure inhibits the mTOR signaling pathway via AMPK in the rat frontal cortex
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Jeon, J. Y., Kim, S. W., Park, K. C., & Yun, M. (2015) · BMC Cancer · doi:10.1186/s12885-015-1640-z · Cited by 22
Odeh, M., Tamir, Y., Haas, T., & Bengal, E. (2019) · FEBS Journal · doi:10.1111/febs.15070 · Cited by 22
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Wang, Y., Wu, N., Li, J., Liang, J., Zhou, D., Cao, Q., Li, X., & Jiang, N. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107162 · Cited by 21
Babygirija, R., Sonsalla, M. M., Mill, J., James, I., Han, J. H., Green, C. L., Calubag, M. F., Wade, G., Tobon, A., Michael, J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49589-z · Cited by 22
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Tezil, T., & Başağa, H. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113196660702 · Cited by 21
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Hou, B., Wang, G., Gao, Q., Wei, Y., Zhang, C., Wang, Y., Huo, Y., Yang, H., Jiang, X., & Xi, Z. (2019) · Scientific Reports · doi:10.1038/s41598-019-47597-4 · Cited by 21
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Liu, H.-T., & Pan, S.-S. (2019) · BioMed Research International · doi:10.1155/2019/5697380 · Cited by 19
König, P., Svrlanska, A., Read, C., Feichtinger, S., & Stamminger, T. (2020) · Journal of Virology · doi:10.1128/jvi.02346-20 · Cited by 18
Kötter, S., & Krüger, M. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.914296 · Cited by 22
Wang, S., Xue, H., Xu, Y., Niu, J., & Zhao, P. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2682-9 · Cited by 19
Dang, X., Wong, N.-K., Xie, Y., Thiyagarajan, V., Mao, F., Zhang, X., Lin, Y. N., Xiang, Z., Li, J., Xiao, S., et al. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00411 · Cited by 19
Zhong, L., Fang, S., Wang, A.-Q., Zhang, Z., Wang, T., Huang, W. H., Zhou, H., Zhang, H., & Yin, Z. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108492 · Cited by 19
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Zhang, Y., Qu, X., & Jiang, L. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.05.132 · Cited by 18
Li, G., Xu, Y., Li, Y., Chang, D., Zhang, P., Ma, Z., Chen, D., You, Y., Huang, X., & Cai, J. (2023) · Pharmaceutical Biology · doi:10.1080/13880209.2023.2168021 · Cited by 18
Bhattacharya, S., Piya, S., Ma, H., Sharma, P., Zhang, Q., Baran, N., Ruvolo, V. R., McQueen, T. J., Davis, R. E., Pourebrahim, R., et al. (2023) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-22-0343 · Cited by 19
Montalvo, R. N., Doerr, V., Kwon, O. S., Talbert, E. E., Yoo, J., Hwang, M., Nguyen, B. L., Christou, D. D., Kavazis, A. N., & Smuder, A. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218105 · Cited by 19
Gao, J., Liang, Y., Wang, Z., Wang, R., & Liu, X. (2020) · PubMed · Cited by 18
Zhang, E., Song, X., Yin, S., Fan, L., Ye, M., & Hu, H. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2017.04.036 · Cited by 18
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Przygrodzka, E., Monaco, C. F., Plewes, M. R., Li, G., Wood, J. R., Cupp, A. S., & Davis, J. S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.723563 · Cited by 17
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Costa, A. J., Oliveira, R. B., Wachilewski, P., Nishino, M. S., Bassani, T. B., Stilhano, R. S., Cerutti, J. M., Nozima, B. H. N., Porto, C. S., Pereira, G. J. S., et al. (2022) · Brain Research · doi:10.1016/j.brainres.2022.148079 · Cited by 17
Huang, H., Wang, T., Wang, L.-P., Huang, Y., Li, W., Wang, J., Hu, Y., & Zhou, Z. (2023) · Experimental Gerontology · doi:10.1016/j.exger.2023.112305 · Cited by 17
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Luo, Q., Zhang, L., Wei, F., Fang, Q., Bao, F., Mi, S., Li, N., Wang, C., Liu, Y., & Tu, C. (2018) · iScience · doi:10.1016/j.isci.2018.04.010 · Cited by 18
Hodson, N. W., Mazzulla, M., Holowaty, M. N. H., Kumbhare, D. A., & Moore, D. R. (2021) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00357.2021 · Cited by 18
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Wang, J., Wen, D., Wang, S., Gao, Y., & Yin, X. (2023) · The FASEB Journal · doi:10.1096/fj.202301312r · Cited by 16
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Pang, J., Yang, H., Feng, X., Wang, Q., Cai, Y., Liu, Z., Wang, C., Wang, F., & Zhang, Y. (2021) · Theriogenology · doi:10.1016/j.theriogenology.2021.01.015 · Cited by 16
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Metadata
- Authors
- Egan, D., Kim, J., Shaw, R. J., & Guan, K.-L.
- Affiliations
- Salk Institute for Biological Studies (US)
- University of California San Diego (US)
- Corresponding author
- Shaw, Reuben J.
- Guan, Kun-Liang
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2011-06
- Volume
- 7
- Issue
- 6
- Pages
- 643-644
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- PMC
- PMC3359466
- OpenAlex
- W2070871404
- Cited by
- 627
- References
- 2
- Citations by year
- 2026: 20 · 2025: 28 · 2024: 51 · 2023: 33 · 2022: 53 · 2021: 61 · 2020: 57 · 2019: 54 · 2018: 49 · 2017: 56 · 2016: 41 · 2015: 34 · 2014: 42 · 2013: 19 · 2012: 25
- FWCI
- 21.69
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Autophagy (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R01CA108941)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- ULK1, autophagy initiation, AMPK, mTORC1, protein phosphorylation, nutrient signaling, glucose deprivation, TOR signaling, kinase regulation
- MeSH terms
- Autophagy-Related Protein-1 Homolog, Mechanistic Target of Rapamycin Complex 1, Adenylate Kinase, Animals, Autophagy, Saccharomycetales, Glucose, Humans, Models, Biological, Phosphorylation, Proteins, Gene Expression Regulation, Fungal, Caenorhabditis elegans, Protein Serine-Threonine Kinases, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Mice, TOR Serine-Threonine Kinases
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